期刊
MICROBIOLOGY AND IMMUNOLOGY
卷 64, 期 10, 页码 657-665出版社
WILEY
DOI: 10.1111/1348-0421.12841
关键词
apoptosis; endoplasmic reticulum stress; receptor; Shiga-toxigenicEscherichia coli; subtilase cytotoxin
资金
- Research Program on Emerging and Reemerging Infectious Diseases from Japan Agency for Medical Research and Development, AMED
- Japan Society for Promotion of Science (JSPS) KAKENHI
- Takeda Science Foundation
Shiga-toxigenicEscherichia coli(STEC) is a major bacterium responsible for disease resulting from foodborne infection, including bloody diarrhea and hemolytic uremic syndrome. STEC produces important virulence factors such as Shiga toxin (Stx) 1 and/or 2. In the STEC family, some locus of enterocyte effacement-negative STEC produce two different types of cytotoxins, namely, Stx2 and subtilase cytotoxin (SubAB). The Stx2 and SubAB cytotoxins are structurally similar and composed of one A subunit and pentamer of B subunits. The catalytically active A subunit of SubAB is a subtilase-like serine protease and specifically cleaves an endoplasmic reticulum (ER) chaperone 78-kDa glucose-regulated protein (GRP78/BiP), a monomeric ATPase that is crucial in protein folding and quality control. The B subunit binds to cell surface receptors. SubAB recognizes sialic carbohydrate-modified cell surface proteins as a receptor. After translocation into cells, SubAB is delivered to the ER, where it cleaves GRP78/BiP. SubAB-catalyzed BiP cleavage induces ER stress, which causes various cell events including inhibition of protein synthesis, suppression of nuclear factor-kappa B activation, apoptotic cell death, and stress granules formation. In this review, we describe SubAB, the SubAB receptor, and the mechanism of cell response to the toxin.
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